CX6A2_RAT
ID CX6A2_RAT Reviewed; 94 AA.
AC P10817;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytochrome c oxidase subunit 6A2, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIa-heart;
DE Short=COXVIAH;
DE Flags: Precursor; Fragment;
GN Name=Cox6a2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2461293; DOI=10.1002/j.1460-2075.1988.tb03083.x;
RA Schlerf A., Droste M., Winter M., Kadenbach B.;
RT "Characterization of two different genes (cDNA) for cytochrome c oxidase
RT subunit VIa from heart and liver of the rat.";
RL EMBO J. 7:2387-2391(1988).
RN [2]
RP SEQUENCE REVISION.
RA Kadenbach B.;
RL Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 10-19.
RC TISSUE=Heart;
RX PubMed=2153407; DOI=10.1016/0005-2728(90)90042-3;
RA Kadenbach B., Stroh A., Becker A., Eckersorn C., Lottspeich F.;
RT "Tissue- and species-specific expression of cytochrome c oxidase isozymes
RT in vertebrates.";
RL Biochim. Biophys. Acta 1015:368-372(1990).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules unsing 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. Plays a role in the assembly and
CC stabilization of complex IV (By similarity).
CC {ECO:0000250|UniProtKB:P32799, ECO:0000250|UniProtKB:P43023}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P32799}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)).
CC {ECO:0000250|UniProtKB:P07471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07471}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07471}.
CC -!- TISSUE SPECIFICITY: Heart/muscle specific isoform.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X12554; CAA31068.1; ALT_INIT; mRNA.
DR PIR; S01157; S01157.
DR AlphaFoldDB; P10817; -.
DR SMR; P10817; -.
DR STRING; 10116.ENSRNOP00000026908; -.
DR CarbonylDB; P10817; -.
DR PhosphoSitePlus; P10817; -.
DR PaxDb; P10817; -.
DR PRIDE; P10817; -.
DR UCSC; RGD:2385; rat.
DR RGD; 2385; Cox6a2.
DR eggNOG; KOG3469; Eukaryota.
DR InParanoid; P10817; -.
DR PhylomeDB; P10817; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:RGD.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00925; Cyt_c_Oxidase_VIa; 1.
DR Gene3D; 4.10.95.10; -; 1.
DR InterPro; IPR001349; Cyt_c_oxidase_su6a.
DR InterPro; IPR018507; Cyt_c_oxidase_su6a_CS.
DR InterPro; IPR036418; Cyt_c_oxidase_su6a_sf.
DR PANTHER; PTHR11504; PTHR11504; 1.
DR Pfam; PF02046; COX6A; 1.
DR PIRSF; PIRSF000277; COX6A1; 1.
DR SUPFAM; SSF81411; SSF81411; 1.
DR PROSITE; PS01329; COX6A; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT <1..9
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2153407"
FT CHAIN 10..94
FT /note="Cytochrome c oxidase subunit 6A2, mitochondrial"
FT /id="PRO_0000006118"
FT TOPO_DOM 10..21
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07471"
FT TRANSMEM 22..46
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07471"
FT TOPO_DOM 47..94
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07471"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 94 AA; 10487 MW; AAF44BDDACEF50A6 CRC64;
PLKVLSRSMA SASKGDHGGA GANTWRLLTF VLALPSVALC SLNCWMHAGH HERPEFIPYH
HLRIRTKPFS WGDGNHTLFH NPHVNPLPTG YEQP
